5O7Z
Crystal Structure of R67A Mutant of alpha-L-arabinofuranosidase Ara51 from Clostridium thermocellum
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000272 | biological_process | polysaccharide catabolic process |
A | 0005737 | cellular_component | cytoplasm |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0031222 | biological_process | arabinan catabolic process |
A | 0046373 | biological_process | L-arabinose metabolic process |
A | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
B | 0000272 | biological_process | polysaccharide catabolic process |
B | 0005737 | cellular_component | cytoplasm |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0031222 | biological_process | arabinan catabolic process |
B | 0046373 | biological_process | L-arabinose metabolic process |
B | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
C | 0000272 | biological_process | polysaccharide catabolic process |
C | 0005737 | cellular_component | cytoplasm |
C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
C | 0031222 | biological_process | arabinan catabolic process |
C | 0046373 | biological_process | L-arabinose metabolic process |
C | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
D | 0000272 | biological_process | polysaccharide catabolic process |
D | 0005737 | cellular_component | cytoplasm |
D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
D | 0031222 | biological_process | arabinan catabolic process |
D | 0046373 | biological_process | L-arabinose metabolic process |
D | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
E | 0000272 | biological_process | polysaccharide catabolic process |
E | 0005737 | cellular_component | cytoplasm |
E | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
E | 0031222 | biological_process | arabinan catabolic process |
E | 0046373 | biological_process | L-arabinose metabolic process |
E | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
F | 0000272 | biological_process | polysaccharide catabolic process |
F | 0005737 | cellular_component | cytoplasm |
F | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
F | 0031222 | biological_process | arabinan catabolic process |
F | 0046373 | biological_process | L-arabinose metabolic process |
F | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue DIO C 601 |
Chain | Residue |
C | PHE25 |
C | GLU27 |
C | TRP97 |
C | TYR244 |
C | GLU292 |
C | LEU319 |
C | GLN352 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue DIO D 601 |
Chain | Residue |
D | TYR244 |
D | GLU292 |
D | TRP296 |
D | GLN352 |
D | PHE25 |
D | GLU27 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue DIO E 601 |
Chain | Residue |
E | GLU27 |
E | GLY71 |
E | ASN72 |
E | TRP97 |
E | GLU173 |
E | TYR244 |
E | GLU292 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue DIO F 601 |
Chain | Residue |
F | GLU27 |
F | GLY71 |
F | ASN72 |
F | TRP97 |
F | GLU173 |
F | TYR244 |
F | GLU292 |
F | TRP296 |
F | GLN352 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:16336192 |
Chain | Residue | Details |
A | GLU173 | |
B | GLU173 | |
C | GLU173 | |
D | GLU173 | |
E | GLU173 | |
F | GLU173 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:16336192 |
Chain | Residue | Details |
A | GLU292 | |
B | GLU292 | |
C | GLU292 | |
D | GLU292 | |
E | GLU292 | |
F | GLU292 |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|Ref.3, ECO:0000305|PubMed:16336192, ECO:0007744|PDB:2C7F, ECO:0007744|PDB:2C8N, ECO:0007744|PDB:5O80, ECO:0007744|PDB:5O82 |
Chain | Residue | Details |
A | GLU27 | |
C | ASN72 | |
C | TYR244 | |
C | GLU292 | |
D | GLU27 | |
D | ASN72 | |
D | TYR244 | |
D | GLU292 | |
E | GLU27 | |
E | ASN72 | |
E | TYR244 | |
A | ASN72 | |
E | GLU292 | |
F | GLU27 | |
F | ASN72 | |
F | TYR244 | |
F | GLU292 | |
A | TYR244 | |
A | GLU292 | |
B | GLU27 | |
B | ASN72 | |
B | TYR244 | |
B | GLU292 | |
C | GLU27 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|Ref.3, ECO:0000305|PubMed:16336192, ECO:0007744|PDB:2C7F, ECO:0007744|PDB:5O82 |
Chain | Residue | Details |
A | ASN172 | |
B | ASN172 | |
C | ASN172 | |
D | ASN172 | |
E | ASN172 | |
F | ASN172 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|Ref.3, ECO:0000305|PubMed:16336192, ECO:0007744|PDB:2C8N, ECO:0007744|PDB:5O80 |
Chain | Residue | Details |
A | GLN352 | |
B | GLN352 | |
C | GLN352 | |
D | GLN352 | |
E | GLN352 | |
F | GLN352 |
site_id | SWS_FT_FI6 |
Number of Residues | 12 |
Details | SITE: Important for substrate recognition => ECO:0000250|UniProtKB:Q9XBQ3 |
Chain | Residue | Details |
A | TRP296 | |
E | GLN352 | |
F | TRP296 | |
F | GLN352 | |
A | GLN352 | |
B | TRP296 | |
B | GLN352 | |
C | TRP296 | |
C | GLN352 | |
D | TRP296 | |
D | GLN352 | |
E | TRP296 |